ID ADH6_YEAST Reviewed; 360 AA. AC Q04894; D6W0E6; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 186. DE RecName: Full=NADP-dependent alcohol dehydrogenase 6 {ECO:0000305}; DE EC=1.1.1.2 {ECO:0000269|PubMed:11742541}; DE AltName: Full=NADP-dependent alcohol dehydrogenase VI; DE AltName: Full=ScADHVI {ECO:0000303|PubMed:11742541}; GN Name=ADH6 {ECO:0000303|PubMed:11742541}; OrderedLocusNames=YMR318C; GN ORFNames=YM9924.10C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; RL Nature 387:90-93(1997). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=11742541; DOI=10.1042/0264-6021:3610163; RA Larroy C., Fernandez M.R., Gonzalez E., Pares X., Biosca J.A.; RT "Characterization of the Saccharomyces cerevisiae YMR318C (ADH6) gene RT product as a broad specificity NADPH-dependent alcohol dehydrogenase: RT relevance in aldehyde reduction."; RL Biochem. J. 361:163-172(2002). RN [4] RP FUNCTION. RX PubMed=12604208; DOI=10.1016/s0009-2797(02)00166-7; RA Larroy C., Rosario Fernandez M., Gonzalez E., Pares X., Biosca J.A.; RT "Properties and functional significance of Saccharomyces cerevisiae RT ADHVI."; RL Chem. Biol. Interact. 143:229-238(2003). RN [5] RP CRYSTALLIZATION. RX PubMed=12554944; DOI=10.1107/s090744490201661x; RA Valencia E., Rosell A., Larroy C., Farres J., Biosca J.A., Fita I., RA Pares X., Ochoa W.F.; RT "Crystallization and preliminary X-ray analysis of NADP(H)-dependent RT alcohol dehydrogenases from Saccharomyces cerevisiae and Rana perezi."; RL Acta Crystallogr. D 59:334-337(2003). RN [6] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [7] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [8] RP FUNCTION. RX PubMed=16652391; DOI=10.1002/yea.1370; RA Petersson A., Almeida J.R., Modig T., Karhumaa K., Hahn-Haegerdal B., RA Gorwa-Grauslund M.F., Liden G.; RT "A 5-hydroxymethyl furfural reducing enzyme encoded by the Saccharomyces RT cerevisiae ADH6 gene conveys HMF tolerance."; RL Yeast 23:455-464(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-359, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [11] {ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0, ECO:0007744|PDB:1Q1N} RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH NADP(+) AND ZN(2+). RX PubMed=15289102; DOI=10.1016/j.jmb.2004.06.037; RA Valencia E., Larroy C., Ochoa W.F., Pares X., Fita I., Biosca J.A.; RT "Apo and Holo structures of an NADPH-dependent cinnamyl alcohol RT dehydrogenase from Saccharomyces cerevisiae."; RL J. Mol. Biol. 341:1049-1062(2004). CC -!- FUNCTION: NADP-dependent, medium-chain alcohol dehydrogenase with a CC broad substrate specificity. Aldehydes exhibited 50-12000 times higher CC catalytic efficiency than the corresponding alcohols, therefore the CC major function of the enzyme is as an aldehyde reductase. The enzyme is CC active towards aromatic and aliphatic (linear and branched-chain) CC aldehydes. The enzyme is very active towards aromatic aldehydes, such CC as cinnamaldehyde, benzaldehyde and substituted benzaldehydes, such as CC veratraldehyde and panisaldehyde. It exhibits low activity towards CC substituted cinnamaldehydes, such as coniferaldehyde and sinapaldehyde. CC The enzyme has no activity with ketones, such as acetone or CC cyclohexanone. For the reverse reaction, linear and branched-chain CC primary alcohols are substrates, whereas very low activity is found CC with secondary alcohols, such as butan-2-ol (PubMed:11742541). The CC enzyme may be physiologically involved in several steps of the lignin CC degradation pathway, initiated by other microorganisms, in the CC synthesis of fusel alcohols, products derived from the aminoacidic CC metabolism, and in the homeostasis of NADP(H) (Probable). Has the CC ability to reduce 5-hydroxymethyl furfural (HMF), a furan derivative CC which is formed during the hydrolysis of lignocellulosic materials, to CC 5-hydroxymethylfurfuryl alcohol, thereby alleviating the inhibition of CC the fermentation of lignocellulose hydrolysates by HMF during fuel CC ethanol production (PubMed:16652391). {ECO:0000269|PubMed:11742541, CC ECO:0000269|PubMed:16652391, ECO:0000305|PubMed:12604208}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH; CC Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.2; CC Evidence={ECO:0000269|PubMed:11742541}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15938; CC Evidence={ECO:0000269|PubMed:11742541}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15939; CC Evidence={ECO:0000269|PubMed:11742541}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) + CC NADPH; Xref=Rhea:RHEA:10392, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731, CC ChEBI:CHEBI:33227, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; CC Evidence={ECO:0000269|PubMed:11742541}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hexan-1-ol + NADP(+) = H(+) + hexanal + NADPH; CC Xref=Rhea:RHEA:58404, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:87393, ChEBI:CHEBI:88528; CC Evidence={ECO:0000269|PubMed:11742541}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-methylbutanol + NADP(+) = 3-methylbutanal + H(+) + NADPH; CC Xref=Rhea:RHEA:18525, ChEBI:CHEBI:15378, ChEBI:CHEBI:15837, CC ChEBI:CHEBI:16638, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; CC Evidence={ECO:0000269|PubMed:11742541}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:15289102}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:15289102}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.172 mM for cinnamaldehyde {ECO:0000269|PubMed:11742541}; CC KM=0.073 mM for veratraldehyde {ECO:0000269|PubMed:11742541}; CC KM=0.152 mM for hexanal {ECO:0000269|PubMed:11742541}; CC KM=0.06 mM for pentanal {ECO:0000269|PubMed:11742541}; CC KM=0.129 mM for 3-methylbutanal {ECO:0000269|PubMed:11742541}; CC KM=0.029 mM for NADPH {ECO:0000269|PubMed:11742541}; CC KM=0.436 mM for cinnamyl alcohol {ECO:0000269|PubMed:11742541}; CC KM=9.1 mM for hexan-1-ol {ECO:0000269|PubMed:11742541}; CC KM=10.5 mM for pentan-1-ol {ECO:0000269|PubMed:12604208}; CC KM=0.061 mM for NADP(+) {ECO:0000269|PubMed:11742541}; CC pH dependence: CC Optimum pH is 7 for the reduction reaction and 10 for the oxidation CC reaction. {ECO:0000269|PubMed:12604208}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11742541}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus CC {ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 21700 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z54141; CAA90836.1; -; Genomic_DNA. DR EMBL; BK006946; DAA10220.1; -; Genomic_DNA. DR PIR; S59311; S59311. DR RefSeq; NP_014051.3; NM_001182831.3. DR PDB; 1PIW; X-ray; 3.00 A; A/B=1-360. DR PDB; 1PS0; X-ray; 3.01 A; A=1-360. DR PDB; 1Q1N; X-ray; 3.15 A; A=1-360. DR PDBsum; 1PIW; -. DR PDBsum; 1PS0; -. DR PDBsum; 1Q1N; -. DR AlphaFoldDB; Q04894; -. DR SMR; Q04894; -. DR BioGRID; 35498; 91. DR DIP; DIP-6308N; -. DR IntAct; Q04894; 4. DR STRING; 4932.YMR318C; -. DR iPTMnet; Q04894; -. DR MaxQB; Q04894; -. DR PaxDb; 4932-YMR318C; -. DR PeptideAtlas; Q04894; -. DR EnsemblFungi; YMR318C_mRNA; YMR318C; YMR318C. DR GeneID; 855368; -. DR KEGG; sce:YMR318C; -. DR AGR; SGD:S000004937; -. DR SGD; S000004937; ADH6. DR VEuPathDB; FungiDB:YMR318C; -. DR eggNOG; KOG0023; Eukaryota. DR GeneTree; ENSGT00940000176642; -. DR HOGENOM; CLU_026673_20_2_1; -. DR InParanoid; Q04894; -. DR OMA; GWGEQKF; -. DR OrthoDB; 5353053at2759; -. DR BioCyc; YEAST:YMR318C-MONOMER; -. DR SABIO-RK; Q04894; -. DR BioGRID-ORCS; 855368; 8 hits in 10 CRISPR screens. DR EvolutionaryTrace; Q04894; -. DR PRO; PR:Q04894; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; Q04894; Protein. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0052675; F:3-methylbutanol:NADP oxidoreductase activity; IEA:RHEA. DR GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IDA:SGD. DR GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IEA:RHEA. DR GO; GO:0033833; F:hydroxymethylfurfural reductase (NADH) activity; IMP:SGD. DR GO; GO:0033845; F:hydroxymethylfurfural reductase (NADPH) activity; IMP:SGD. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006066; P:alcohol metabolic process; IDA:SGD. DR GO; GO:0006081; P:cellular aldehyde metabolic process; IDA:SGD. DR GO; GO:0033859; P:furaldehyde metabolic process; IMP:SGD. DR CDD; cd05283; CAD1; 1. DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR013149; ADH-like_C. DR InterPro; IPR013154; ADH-like_N. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR047109; CAD-like. DR InterPro; IPR011032; GroES-like_sf. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1. DR PANTHER; PTHR42683:SF39; NADP-DEPENDENT ALCOHOL DEHYDROGENASE 6-RELATED; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; GroES-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Metal-binding; NADP; Nucleus; Oxidoreductase; KW Phosphoprotein; Reference proteome; Zinc. FT CHAIN 1..360 FT /note="NADP-dependent alcohol dehydrogenase 6" FT /id="PRO_0000160734" FT BINDING 46 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1Q1N" FT BINDING 47 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0" FT BINDING 51 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW" FT BINDING 68 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1Q1N" FT BINDING 100 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0, FT ECO:0007744|PDB:1Q1N" FT BINDING 103 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0, FT ECO:0007744|PDB:1Q1N" FT BINDING 106 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0, FT ECO:0007744|PDB:1Q1N" FT BINDING 114 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0, FT ECO:0007744|PDB:1Q1N" FT BINDING 163 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1Q1N" FT BINDING 188 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW" FT BINDING 190 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0" FT BINDING 191 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0" FT BINDING 210 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0" FT BINDING 211 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0" FT BINDING 215 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0" FT BINDING 250 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW" FT BINDING 252 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0" FT BINDING 255 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0" FT BINDING 256 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PS0" FT BINDING 275 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PS0" FT BINDING 277 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0" FT BINDING 298 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW" FT BINDING 299 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0" FT BINDING 301 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0" FT BINDING 348 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:15289102, FT ECO:0007744|PDB:1PIW" FT MOD_RES 131 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 359 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT TURN 3..5 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 7..12 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 15..17 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 22..26 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 35..45 FT /evidence="ECO:0007829|PDB:1PIW" FT HELIX 47..53 FT /evidence="ECO:0007829|PDB:1PIW" FT TURN 54..57 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 70..77 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 90..93 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 95..98 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 101..103 FT /evidence="ECO:0007829|PDB:1Q1N" FT HELIX 104..107 FT /evidence="ECO:0007829|PDB:1PIW" FT HELIX 111..113 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 118..122 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 134..142 FT /evidence="ECO:0007829|PDB:1PIW" FT HELIX 143..145 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:1PIW" FT HELIX 155..158 FT /evidence="ECO:0007829|PDB:1PIW" FT HELIX 159..162 FT /evidence="ECO:0007829|PDB:1PIW" FT HELIX 164..174 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 182..186 FT /evidence="ECO:0007829|PDB:1PIW" FT HELIX 190..202 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 205..213 FT /evidence="ECO:0007829|PDB:1PIW" FT HELIX 216..221 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 225..229 FT /evidence="ECO:0007829|PDB:1PIW" FT HELIX 230..232 FT /evidence="ECO:0007829|PDB:1PIW" FT HELIX 236..239 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 244..249 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 254..256 FT /evidence="ECO:0007829|PDB:1PS0" FT TURN 259..261 FT /evidence="ECO:0007829|PDB:1PIW" FT HELIX 262..265 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 266..274 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 284..286 FT /evidence="ECO:0007829|PDB:1PIW" FT HELIX 288..290 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 295..298 FT /evidence="ECO:0007829|PDB:1PIW" FT HELIX 304..316 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 323..329 FT /evidence="ECO:0007829|PDB:1PIW" FT HELIX 330..342 FT /evidence="ECO:0007829|PDB:1PIW" FT STRAND 346..352 FT /evidence="ECO:0007829|PDB:1PIW" FT HELIX 355..358 FT /evidence="ECO:0007829|PDB:1PIW" SQ SEQUENCE 360 AA; 39618 MW; 3F785BE0C5ED8CF1 CRC64; MSYPEKFEGI AIQSHEDWKN PKKTKYDPKP FYDHDIDIKI EACGVCGSDI HCAAGHWGNM KMPLVVGHEI VGKVVKLGPK SNSGLKVGQR VGVGAQVFSC LECDRCKNDN EPYCTKFVTT YSQPYEDGYV SQGGYANYVR VHEHFVVPIP ENIPSHLAAP LLCGGLTVYS PLVRNGCGPG KKVGIVGLGG IGSMGTLISK AMGAETYVIS RSSRKREDAM KMGADHYIAT LEEGDWGEKY FDTFDLIVVC ASSLTDIDFN IMPKAMKVGG RIVSISIPEQ HEMLSLKPYG LKAVSISYSA LGSIKELNQL LKLVSEKDIK IWVETLPVGE AGVHEAFERM EKGDVRYRFT LVGYDKEFSD //